N-TIMP

Tessonnier J-P, Rosenthal D, Hansen TW, Hess C, Schuster ME, Blume R, Girgsdies F, Pfander N, Timpe O, Su DS, Schlogl R. Analysis of the structure and chemical properties of some commercial carbon nanostructures. Carbon. 2009 47(7) 1779-1798. 

V. Semenchenko, K. Brew, S. R. Van Doren, Increased backbone mobility in beta-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3,... 

The effects of pH and molecular charge on dipolar coupling interactions of solutes in skeletal muscle have been studied by Asllani et by the use of DQF and H NMR spectroscopy. Global orientation of bound MMP-3 and N-TIMP-in solution via residual dipolar Dhn and Dhc couplings has been studied by Arumugam and Van Doren. ... 

Giersing BK, Rae MT, CarbalhdoBrea M, Williamson RA, Blower PJ. Synthesis and characterization of lllIn-DTPA-N-TIMP-2 a radiopharmaceutical for imaging matrix metalloproteinase expression. Bioconjug Chem 2001 12 964-971. 

Staphylococcal nuclease with substrate analogues Stromelysin domain with N-TIMP-2 inhibitor Stromelysin with nonpeptide inhibitors Thioredoxin with NFkP peptide Topoisomerase-I domain with DNA Trp repressor with DNA Trypsin with proteinase inhibitors Urbs 1 with DNA... 

Emenaker NJ, Calaf GM, Cox D, Basson MD, Qureshi N. (2001) Short-chain fatty acids inhibit invasive human colon cancer by modulating uPA, TIMP-1, TlMP-2, mntant p53, Bcl-2, BAX, p21 and PCNA protein expression in an in vitro cell cnltnre model. JNutr 131 3041S-3046S. 

Timpe H-J (1990) Photoinduced Electron Transfer Polymerization. 155 167-198 TobeY (1994) Strained [n]Cyclophanes. 172 1-40 Tolentino H, see Fontaine A (1989) 151 179-203... 

Heteroaromatic N-Imines H.-J. Timpe, Adv. Heterocycl. Chem., 1974,17, 213-255. Chemistry of the Heterocyclic N-Oxides , A. R. Katritzky and J. M. Lagowski, Academic Press, New York, 1971. 

W. Timpe, K. Dax, N. Wolf, and H. Weidmann, 3-Desoxyhex-2-enono-1,4-lactone aus D-hexofuran(osid)urono-6,3-lactonen, Carbohydr. Res., 39 (1975) 53-60. 

Werner H, Timpe O, Herein D, Uchida Y, Pfander N, Wild U, Schlogl R, Catal. Lett., 44 153, 1997. 

TIMPs inhibit matrix metaiioproteases (MMPs) via a two-step mechanism in a manner somewhat similar to that of cystatins (Fig. 3). While the N-terminal residues of cystatins bind to the nonprime side of cysteine proteases, TIMPs N-termini bind in the P1-P3 pockets of the protease, coordinate the catalytic... 

Zn + ion, and exclude a catalytic water molecule from the active site. Meanwhile a second loop of the TIMP binds in both the P3 and the P2 pockets, and it binds to the N-terminus of the MMP. Despite the similarities in mechanistic architecture between TIMPs and cystatins (hairpin loops and N-terminal residues in substrate binding pockets), TIMPs interfere with the catalytic machinery of MMPs by chelating the catalytic Zn + (5). 

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